Evidence map›Paper›PMID 12829459›Full record

ArticleBiophysical journal2003

Kinetics from nonequilibrium single-molecule pulling experiments.

Gerhard Hummer, Attila Szabo

Abstract readComparative StudyEvaluation StudyValidation Study
In one paragraph

Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 118 papers.

0numbers the graph read from it
0cells of the map it votes in
118citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

118 citing papers in PubMed.

  1. Single-Molecule Force Spectroscopy: Experiments, Analysis, and Simulations.Methods in molecular biology (Clifton, N.J.) · 2027
    Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
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  8. Chemifriction and Superlubricity: Friends or Foes?The journal of physical chemistry letters · 2025
    Article
  9. Article
  10. Article
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  12. Article
  13. Article
  14. Article
  15. Article
  16. Force Dependent Barriers from Analytic Potentials within Elastic Environments.Chemphyschem : a European journal of chemical physics and physical chemistry · 2022
    Article
  17. Article
  18. Article
  19. Article
  20. Article

58 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Gerhard HummerLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, USA. hummer@helix.nih.gov
Attila Szabo

Funding

Theoretical Studies On The Dynamic Aspects Of Macromolecular FunctionZIADK029019 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI SZABO, ATTILA · 2009 to 2024
$15.0M
Theory and simulation of protein dynamics, folding, and functionZIADK029033 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI HUMMER, GERHARD · 2009 to 2013
$3.3M
Theory &simulation of protein dynamics, folding,&functZ01DK029033 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI HUMMER, GERHARD · 2000 to 2008
$960k
THEORETICAL STUDIES ON THE DYNAMIC ASPECTS OF MACROMOLECULAR FUNCTIONZ01DK029019 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI SZABO, ATTILA · 1986 to 2008
$543k
6 · The paper itself

Abstract

Mechanical forces exerted by laser tweezers or atomic force microscopes can be used to drive rare transitions in single molecules, such as unfolding of a protein or dissociation of a ligand. The phenomenological description of pulling experiments based on Bell's expression for the force-induced rupture rate is found to be inadequate when tested against computer simulations of a simple microscopic model of the dynamics. We introduce a new approach of comparable complexity to extract more accurate kinetic information about the molecular events from pulling experiments. Our procedure is based on the analysis of a simple stochastic model of pulling with a harmonic spring and encompasses the phenomenological approach, reducing to it in the appropriate limit. Our approach is tested against computer simulations of a multimodule titin model with anharmonic linkers and then an illustrative application is made to the forced unfolding of I27 subunits of the protein titin. Our procedure to extract kinetic information from pulling experiments is simple to implement and should prove useful in the analysis of experiments on a variety of systems.

Indexed as

Energy TransferModels, MolecularComputer SimulationConnectinCrystallographyKineticsLasersMicromanipulationMicroscopy, Atomic ForceMolecular ConformationMotionMuscle ProteinsNanotechnologyPhysical StimulationProtein ConformationProtein DenaturationConnectinMuscle ProteinsProtein Kinases

Identifiers

PMID12829459
PMCPMC1303060

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.